BRENDA - Enzyme Database
show all sequences of 1.2.5.3

The aerobic CO dehydrogenase from Oligotropha carboxidovorans

Hille, R.; Dingwall, S.; Wilcoxen, J.; J. Biol. Inorg. Chem. 20, 243-251 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
the enzyme is encoded by the coxMSL structural genes in the megaplasmid-localized coxBCMSLDEFGHIK gene cluster
Oligotropha carboxidovorans
Crystallization (Commentary)
Crystallization
Organism
enzyme in complex with inhibitor n-butylisonitrile, PDB ID 1N62, structure analysis
Oligotropha carboxidovorans
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
thiol inhibition of CO dehydrogenase
Oligotropha carboxidovorans
n-butylisonitrile
-
Oligotropha carboxidovorans
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
the enzyme's physiological position is on the inner side of the cytoplasmic membrane, membrane associated, if not membrane-integral
Oligotropha carboxidovorans
16020
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
-
Oligotropha carboxidovorans
Molybdenum
-
Oligotropha carboxidovorans
[2Fe-2S] cluster
two [2Fe-2S] iron-sulfur clusters in the small subunit
Oligotropha carboxidovorans
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
CO + ubiquinone + H2O
Oligotropha carboxidovorans
ubiquinone is the likely physiological oxidant for CO dehydrogenase
CO2 + ubiquinol
-
-
?
additional information
Oligotropha carboxidovorans
air-stable CO dehydrogenase having a binuclear molybdenum- and copper-containing active site catalyzes the first step in this process, the oxidation of CO to CO2, with the reducing equivalents. Enzyme reduction and reactivity with H2, kinetics, overview
?
-
-
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Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Oligotropha carboxidovorans
P19919 and P19920 and P19921
genes coxL, coxM, and coxS; the enzyme is encoded by coxMSL structural genes in the megaplasmid-localized coxBCMSLDEFGHIK gene cluster
-
Reaction
Reaction
Commentary
Organism
CO + a quinone + H2O = CO2 + a quinol
proposed reaction mechanisms for CO dehydrogenase, the rate-limiting step for overall turnover resides in the reductive half-reaction, reoxidation of reduced enzyme by quinones occurs at the FAD site
Oligotropha carboxidovorans
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
CO + 1,2-naphthoquinone-4-sulfonic acid + H2O
-
736514
Oligotropha carboxidovorans
CO2 + 1,2-naphthoquinol-4-sulfonic acid
-
-
-
?
CO + 1,4-naphthoquinone + H2O
-
736514
Oligotropha carboxidovorans
CO2 + 1,4-naphthoquinol
-
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-
?
CO + a quinone + H2O
-
736514
Oligotropha carboxidovorans
CO2 + a quinol
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?
CO + benzoquinone + H2O
-
736514
Oligotropha carboxidovorans
CO2 + benzoquinol
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?
CO + ubiquinone + H2O
ubiquinone is the likely physiological oxidant for CO dehydrogenase
736514
Oligotropha carboxidovorans
CO2 + ubiquinol
-
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-
?
additional information
air-stable CO dehydrogenase having a binuclear molybdenum- and copper-containing active site catalyzes the first step in this process, the oxidation of CO to CO2, with the reducing equivalents. Enzyme reduction and reactivity with H2, kinetics, overview
736514
Oligotropha carboxidovorans
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
heterohexamer
(abc)2 structure, each protomer of the enzyme has a small subunit (CoxS, 18 kDa) with two [2Fe-2S] iron-sulfur clusters, a medium subunit (CoxM, 30 kDa) that possesses FAD, and a large subunit (CoxL, 89 kDa) that has the active site binuclear center
Oligotropha carboxidovorans
Cofactor
Cofactor
Commentary
Organism
Structure
benzoquinone
-
Oligotropha carboxidovorans
FAD
located in the medium subunit
Oligotropha carboxidovorans
molybdopterin cofactor
the structure of the active site binuclear center of CO dehydrogenase in its oxidized form, overview. The oxidized Mo(VI) ion has the distorted square-pyramidal coordination geometry seen in other members of the xanthine oxidase family of molybdenum-containing enzymes, with an apical Mo=O and an equatorial plane consisting of a second Mo=O group rather than the catalytically labile Mo-OH seen in other family members and two sulfurs from a pyranopterin cofactor that is common to all molybdenum and tungsten enzymes. The pyranopterin cofactor is present as the dinucleotide of cytosine
Oligotropha carboxidovorans
quinone
quinone cofactors interact with CODH at its FAD site
Oligotropha carboxidovorans
ubiquinone-1
-
Oligotropha carboxidovorans
Cloned(Commentary) (protein specific)
Commentary
Organism
the enzyme is encoded by the coxMSL structural genes in the megaplasmid-localized coxBCMSLDEFGHIK gene cluster
Oligotropha carboxidovorans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
benzoquinone
-
Oligotropha carboxidovorans
FAD
located in the medium subunit
Oligotropha carboxidovorans
molybdopterin cofactor
the structure of the active site binuclear center of CO dehydrogenase in its oxidized form, overview. The oxidized Mo(VI) ion has the distorted square-pyramidal coordination geometry seen in other members of the xanthine oxidase family of molybdenum-containing enzymes, with an apical Mo=O and an equatorial plane consisting of a second Mo=O group rather than the catalytically labile Mo-OH seen in other family members and two sulfurs from a pyranopterin cofactor that is common to all molybdenum and tungsten enzymes. The pyranopterin cofactor is present as the dinucleotide of cytosine
Oligotropha carboxidovorans
quinone
quinone cofactors interact with CODH at its FAD site
Oligotropha carboxidovorans
ubiquinone-1
-
Oligotropha carboxidovorans
Crystallization (Commentary) (protein specific)
Crystallization
Organism
enzyme in complex with inhibitor n-butylisonitrile, PDB ID 1N62, structure analysis
Oligotropha carboxidovorans
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
thiol inhibition of CO dehydrogenase
Oligotropha carboxidovorans
n-butylisonitrile
-
Oligotropha carboxidovorans
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
the enzyme's physiological position is on the inner side of the cytoplasmic membrane, membrane associated, if not membrane-integral
Oligotropha carboxidovorans
16020
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
-
Oligotropha carboxidovorans
Molybdenum
-
Oligotropha carboxidovorans
[2Fe-2S] cluster
two [2Fe-2S] iron-sulfur clusters in the small subunit
Oligotropha carboxidovorans
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
CO + ubiquinone + H2O
Oligotropha carboxidovorans
ubiquinone is the likely physiological oxidant for CO dehydrogenase
CO2 + ubiquinol
-
-
?
additional information
Oligotropha carboxidovorans
air-stable CO dehydrogenase having a binuclear molybdenum- and copper-containing active site catalyzes the first step in this process, the oxidation of CO to CO2, with the reducing equivalents. Enzyme reduction and reactivity with H2, kinetics, overview
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
CO + 1,2-naphthoquinone-4-sulfonic acid + H2O
-
736514
Oligotropha carboxidovorans
CO2 + 1,2-naphthoquinol-4-sulfonic acid
-
-
-
?
CO + 1,4-naphthoquinone + H2O
-
736514
Oligotropha carboxidovorans
CO2 + 1,4-naphthoquinol
-
-
-
?
CO + a quinone + H2O
-
736514
Oligotropha carboxidovorans
CO2 + a quinol
-
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-
?
CO + benzoquinone + H2O
-
736514
Oligotropha carboxidovorans
CO2 + benzoquinol
-
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-
?
CO + ubiquinone + H2O
ubiquinone is the likely physiological oxidant for CO dehydrogenase
736514
Oligotropha carboxidovorans
CO2 + ubiquinol
-
-
-
?
additional information
air-stable CO dehydrogenase having a binuclear molybdenum- and copper-containing active site catalyzes the first step in this process, the oxidation of CO to CO2, with the reducing equivalents. Enzyme reduction and reactivity with H2, kinetics, overview
736514
Oligotropha carboxidovorans
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
heterohexamer
(abc)2 structure, each protomer of the enzyme has a small subunit (CoxS, 18 kDa) with two [2Fe-2S] iron-sulfur clusters, a medium subunit (CoxM, 30 kDa) that possesses FAD, and a large subunit (CoxL, 89 kDa) that has the active site binuclear center
Oligotropha carboxidovorans
General Information
General Information
Commentary
Organism
evolution
despite the unique nature of the binuclear active site of CO dehydrogenase the enzyme is clearly a member of the xanthine oxidase family of molybdenum-containing enzymes
Oligotropha carboxidovorans
malfunction
thiol inhibition of CO dehydrogenase may be a physiologically important mechanism of enzyme regulation
Oligotropha carboxidovorans
metabolism
four other genes (coxB, coxC, coxH and coxK) are predicted to encode proteins possessing one (CoxB) to as many as nine (CoxK) transmembrane helices, one or more of which are likely to be involved in anchoring CO dehydrogenase to its physiological position on the inner side of the cytoplasmic membrane
Oligotropha carboxidovorans
additional information
the enzyme possesses a deeply buried binuclear center of CO dehydrogenase activity
Oligotropha carboxidovorans
General Information (protein specific)
General Information
Commentary
Organism
evolution
despite the unique nature of the binuclear active site of CO dehydrogenase the enzyme is clearly a member of the xanthine oxidase family of molybdenum-containing enzymes
Oligotropha carboxidovorans
malfunction
thiol inhibition of CO dehydrogenase may be a physiologically important mechanism of enzyme regulation
Oligotropha carboxidovorans
metabolism
four other genes (coxB, coxC, coxH and coxK) are predicted to encode proteins possessing one (CoxB) to as many as nine (CoxK) transmembrane helices, one or more of which are likely to be involved in anchoring CO dehydrogenase to its physiological position on the inner side of the cytoplasmic membrane
Oligotropha carboxidovorans
additional information
the enzyme possesses a deeply buried binuclear center of CO dehydrogenase activity
Oligotropha carboxidovorans
Other publictions for EC 1.2.5.3
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
736514
Hille
The aerobic CO dehydrogenase f ...
Oligotropha carboxidovorans
J. Biol. Inorg. Chem.
20
243-251
2015
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735935
Stein
Orbital contributions to CO ox ...
Hydrogenophaga pseudoflava, Oligotropha carboxidovorans
Chem. Commun. (Camb.)
50
1104-1106
2014
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736513
Pelzmann
Insights into the posttranslat ...
Oligotropha carboxidovorans
J. Biol. Inorg. Chem.
19
1399-1414
2014
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736437
Wilcoxen
The hydrogenase activity of th ...
Oligotropha carboxidovorans
J. Biol. Chem.
288
36052-36060
2013
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725197
Wilcoxen
Substitution of silver for cop ...
Oligotropha carboxidovorans
J. Am. Chem. Soc.
133
12934-12936
2011
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735667
Wilcoxen
Reaction of the molybdenum- an ...
, Oligotropha carboxidovorans ATCC 49405
Biochemistry
50
1910-1916
2011
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725052
Nishimura
-
Purification and characterizat ...
Aeropyrum pernix, Aeropyrum pernix TB5
Fish. Sci.
76
999-1006
2010
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725392
Zhang
Kinetic and spectroscopic stud ...
Oligotropha carboxidovorans
J. Biol. Chem.
285
12571-12578
2010
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736301
Gourlay
Paramagnetic active site model ...
Oligotropha carboxidovorans
J. Am. Chem. Soc.
128
2164-2165
2006
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736512
Resch
Structural and functional reco ...
Oligotropha carboxidovorans, Oligotropha carboxidovorans DSM 1227
J. Biol. Inorg. Chem.
10
518-528
2005
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390484
Lorite
Carbon monoxide dehydrogenase ...
Bradyrhizobium japonicum, Bradyrhizobium japonicum 110spc4
Appl. Environ. Microbiol.
66
1871-1876
2000
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656481
Hanzelmann
The effect of intracellular mo ...
Hydrogenophaga pseudoflava, Hydrogenophaga pseudoflava DSM 1084
J. Mol. Biol.
301
1221-1235
2000
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736397
Gremer
Binding of flavin adenine dinu ...
Oligotropha carboxidovorans, Oligotropha carboxidovorans DSM 1227
J. Biol. Chem.
275
1864-1872
2000
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390482
Dobbek
Crystal structure and mechanis ...
Oligotropha carboxidovorans
Proc. Natl. Acad. Sci. USA
96
8884-8889
1999
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390483
Kang
Cloning and molecular characte ...
Hydrogenophaga pseudoflava, Hydrogenophaga pseudoflava DSM 1084
J. Bacteriol.
181
5581-5590
1999
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1
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3
3
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2
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1
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1
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2
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1
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3
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1
1
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390479
Schubel
Molecular characterization of ...
Oligotropha carboxidovorans, Oligotropha carboxidovorans OM5
J. Bacteriol.
177
2197-2203
1995
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